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FPG_PSEPF
ID   FPG_PSEPF               Reviewed;         270 AA.
AC   Q3K566;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
DE            Short=Fapy-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
DE            EC=3.2.2.23 {ECO:0000255|HAMAP-Rule:MF_00103};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
DE            Short=AP lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
DE            EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00103};
GN   Name=mutM {ECO:0000255|HAMAP-Rule:MF_00103};
GN   Synonyms=fpg {ECO:0000255|HAMAP-Rule:MF_00103};
GN   OrderedLocusNames=Pfl01_5351;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC       or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC       removes damaged bases. Has a preference for oxidized purines, such as
CC       7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase
CC       activity and introduces nicks in the DNA strand. Cleaves the DNA
CC       backbone by beta-delta elimination to generate a single-strand break at
CC       the site of the removed base with both 3'- and 5'-phosphates.
CC       {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00103};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00103};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00103}.
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DR   EMBL; CP000094; ABA77088.1; -; Genomic_DNA.
DR   RefSeq; WP_011336398.1; NC_007492.2.
DR   AlphaFoldDB; Q3K566; -.
DR   SMR; Q3K566; -.
DR   STRING; 205922.Pfl01_5351; -.
DR   PRIDE; Q3K566; -.
DR   EnsemblBacteria; ABA77088; ABA77088; Pfl01_5351.
DR   KEGG; pfo:Pfl01_5351; -.
DR   eggNOG; COG0266; Bacteria.
DR   HOGENOM; CLU_038423_1_1_6; -.
DR   OMA; GVHLRMT; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   Gene3D; 3.20.190.10; -; 1.
DR   HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   TIGRFAMs; TIGR00577; fpg; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW   Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..270
FT                   /note="Formamidopyrimidine-DNA glycosylase"
FT                   /id="PRO_0000228459"
FT   ZN_FING         236..270
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        2
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        3
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        58
FT                   /note="Proton donor; for beta-elimination activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        260
FT                   /note="Proton donor; for delta-elimination activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   BINDING         91
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   BINDING         110
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   BINDING         151
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
SQ   SEQUENCE   270 AA;  30247 MW;  EC5CCF156EF7A8E2 CRC64;
     MPELPEVETT RRGIAPHLEG QRVSRVIVRD RRLRWPIPED LDVRLSGQRI VLVERRAKYL
     LINAEVGTLI SHLGMSGNLR LVEVGMPAAK HEHVDIELES GLALRYTDPR RFGAMLWSND
     PLNHELLIRL GPEPLTDLFD GERLYQLSRG RSMAVKPFIM DNAVVVGVGN IYATEALFAA
     GIDPRREAKG ISRARYLKLA IEIKRILAAA IERGGTTLRD FIGGDGQPGY FQQELFVYGR
     GGEHCKVCGT GLREMKLGQR ASVWCPRCQS
 
 
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